ReliaTech

ReliaTech GmbH is a Germany-based biotechnology company specializing in the production of high-quality reagents for research in angiogenesis, lymphangiogenesis, and cell signaling. The company was founded with a mission to provide reliable and high-purity cytokines, growth factors, and antibodies to support scientific discoveries in biomedical research.

Product Portfolio

Cytokines & Growth Factors – Recombinant proteins essential for cell signaling and immune response research.
Antibodies – High-specificity antibodies for detecting and analyzing protein interactions.
ELISA Kits – Ready-to-use kits for quantifying biomolecules in various biological samples.
Customized Services – Including protein production, assay development, and contract research.

Commitment to Quality

ReliaTech operates under ISO 9001:2015 certification, ensuring that all products meet rigorous quality and reproducibility standards. Their expertise in protein biochemistry and molecular biology allows them to deliver precise and consistent reagents for academic and industrial laboratories worldwide.

Global Impact

With a strong reputation in the biotech and pharmaceutical industries, ReliaTech serves research institutions, universities, and pharmaceutical companies across the globe, contributing to advancements in drug discovery, cancer research, and regenerative medicine.

Browse ReliaTech Products

4-1BB Ligand/TNFSF9 Protein (human hFc Tag)

SKU: M60-192-L100|Size: 100 µg

4-1BB receptor

SKU: 102-P100G|Size: 100 µg

4-1BB receptor, soluble

SKU: S01-039|Size: 20 µg

4-1BBL

SKU: 100-001S|Size: 5 µg

4-1BBL / CD137L / TNFSF9 Protein (His Tag)

SKU: M60-193-L50|Size: 50 µg

ABCG2 (CD338)

SKU: 101-M10|Size: 100 µg

ACE

SKU: 101-M200|Size: 100 µg

ACE-2

SKU: SFC-002S|Size: 5 µg

ADAM-10

SKU: 103-M300|Size: 50 µg

ADAM-15

SKU: 103-M301|Size: 100 µg

ADAM-17

SKU: 101-M207|Size: 100 µg

ADAM-19

SKU: 103-M302|Size: 100 µg

ADAM-8

SKU: 101-M208|Size: 100 µg

ADAM-9

SKU: 103-M213|Size: 100 µg

ADAMTS4

SKU: 101-M210|Size: 100 µg

ADAMTSL-1

SKU: 101-M211|Size: 100 µg

AGGF1

SKU: 102-PA13|Size: 200 µg

AGGF1 (fragment) Recombinant Protein

SKU: 400-025|Size: 5 µg

AIMP1 / EMAP2 / SCYE1 Protein (His Tag)

SKU: 600-002-L100|Size: 100 µg

AITRL

SKU: 100-122|Size: 20 µg

AKT2

SKU: 101-M106|Size: 50 µg

AKT3

SKU: 101-M107|Size: 50 µg

ALCAM/CD166

SKU: 101-M11|Size: 100 µg

ALK1

SKU: 103-M95|Size: 100 µg

ALK2 (Activin R1A)

SKU: 101-M173|Size: 50 µg

ALK3 (BMP R1A)

SKU: 101-M174|Size: 50 µg

ALK4 (Activin R1B)

SKU: 103-M212|Size: 100 µg

ALK5

SKU: 103-M96|Size: 100 µg

ALK6 (BMP R1B)

SKU: 101-M176|Size: 50 µg

ALPL

SKU: 101-M105|Size: 50 µg

ALS

SKU: 103-M304|Size: 100 µg

AMIGO2

SKU: 101-M119|Size: 50 µg

APRIL

SKU: 100-379|Size: 10 µg

Activin R2A

SKU: 101-M171|Size: 100 µg

Activin R2B

SKU: 101-M172|Size: 50 µg

Activin-A

SKU: 100-012|Size: 10 µg

Activin-A, animal-free

SKU: 100-310-AF|Size: 10 µg

Activin-B

SKU: 101-M203|Size: 50 µg

Activin-C

SKU: 101-M204|Size: 100 µg

Adiponectin

SKU: 102-P102|Size: 100 µg

Adiponectin (Acrp30)

SKU: M10-009|Size: 25 µg

AgRP

SKU: 101-M214|Size: 100 µg

Aggrecan

SKU: 101-M213|Size: 100 µg

Alkaline Phosphatase (ALPP)

SKU: 101-M101|Size: 50 µg

Alpha FAP

SKU: 101-M103|Size: 50 µg

Alpha-fetoprotein (AFP)

SKU: 101-M104|Size: 50 µg

Aminopeptidase

SKU: 100-401|Size: 500 µg

Aminopeptidase P

SKU: 104-M01|Size: 100 µg

Amphiregulin

SKU: M10-019|Size: 50 µg

Amphiregulin (98aa)

SKU: 100-393S|Size: 10 µg

Angiogenin

SKU: 101-M152|Size: 50 µg

Angiopoietin like-1

SKU: 101-M218|Size: 100 µg

Angiopoietin like-2

SKU: 101-M219|Size: 50 µg

Angiopoietin-1 / Ang-1

SKU: 300-048|Size: 20 µg

Angiopoietin-2 / Ang-2

SKU: 300-050|Size: 20 µg

Angiopoietin-3

SKU: 103-M215|Size: 100 µg

Angiopoietin-4

SKU: 101-M127|Size: 100 µg

Angiopoietin-like protein 2

SKU: 103-M306|Size: 100 µg

Angiopoietin-like protein 3

SKU: 100-402|Size: 50 µg

Angiopoietin-like-Protein-7 (ANGPTL7)

SKU: 101-M133|Size: 100 µg

Angiostatin

SKU: 101-M220|Size: 100 µg

Angiotensin-converting Enzyme (CD143)

SKU: 103-M211|Size: 100 µg

Anti-Human Podoplanin Antibody

SKU: 101-M40-PE|Size: 50 µg

Anti-Human TIE-2-FITC Antibody

SKU: 101-M54S-FITC|Size: 25 µg

Anti-Human TIE-2-PE Antibody

SKU: 101-M54S-PE|Size: 25 µg

Anti-Human VEGFR-2/KDR-FITC Antibody

SKU: 101-M20S-FITC|Size: 25 µg

Anti-Mouse AgRP Antibody

SKU: 103-M303|Size: 100 µg

Anti-Mouse CD105/Endoglin Antibody

SKU: 103-M60-PE|Size: 50 µg

Apo-SAA

SKU: 100-127|Size: 50 µg

Apo-SAA1

SKU: 100-387|Size: 50 µg

Apo-SAA1 (Animal Free)

SKU: 100-387-AF|Size: 50 µg

ApoA-I

SKU: 100-123|Size: 100 µg

ApoE2

SKU: 100-124S|Size: 100 µg

ApoE3

SKU: 100-125|Size: 500 µg

ApoE4

SKU: 100-126S|Size: 100 µg

Apolipoprotein A-I/ApoAI Protein (His-tag)

SKU: 600-004-L1000|Size: 1000 µg

Apolipoprotein A-I/ApoAI Protein (hFc-tag)

SKU: 600-003-L100|Size: 100 µg

Arg-C, Enzymogenes

SKU: 100-403|Size: 20 µg

Arginase 1

SKU: 101-M136|Size: 50 µg

Arginine Deiminase (ADI)

SKU: 100-404|Size: 20 µg

Armenian Hamster Anti-Mouse TNF R1 Monoclonal Antibody

SKU: 103-M132|Size: 100 µg

Armenian Hamster Anti-Mouse TNF R2 Monoclonal Antibody

SKU: 103-M134|Size: 100 µg

Armenian hamster Anti-Mouse IFN gamma Receptor-2 Monoclonal Antibody

SKU: 103-M401|Size: 100 µg

Artemin

SKU: M10-129S|Size: 5 µg

Artemin (Animal Free)

SKU: 100-128S-AF|Size: 5 µg

Artemin / ARTN Protein (hFc Tag)

SKU: M60-004-L100|Size: 100 µg

Axl

SKU: 103-M158|Size: 100 µg

Azurocidin/HBP

SKU: 101-M223|Size: 100 µg

B7-1 Fc, soluble

SKU: S01-006S|Size: 20 µg

B7-2 Fc, soluble

SKU: S01-007S|Size: 20 µg

B7-H1/PD-L1 Fc

SKU: 102-P23|Size: 100 µg

B7-H2

SKU: 101-M225|Size: 100 µg

B7-H2 Fc

SKU: 100-017S|Size: 20 µg

B7-H3

SKU: 101-M226|Size: 50 µg

BACE-1

SKU: 101-M227|Size: 50 µg

BAFF

SKU: 100-002|Size: 20 µg

BAFF (Animal Free)

SKU: 100-002S-AF|Size: 5 µg

BAFF receptor, soluble

SKU: S01-038S|Size: 10 µg

BAFFR / TNFRSF13C (Fc & AVI Tag), Biotinylated

SKU: 600-275-L100|Size: 100 µg

BAFFR / TNFRSF13C (hFc & AVI Tag), Biotinylated

SKU: 600-275-L20|Size: 20 µg

Resources & Documents

ReliaTech Customer Service

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2025 Broschüre Cytokine 2 DINA5 FSC

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2025 Broschüre Cytokine 1 DINA5 FSC

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Recent Breakthroughs

Metabolomic insights into Lyme neuroborreliosis: Exploring cerebrospinal fluid for diagnostic clues.

Kuukkanen I, Pietikäinen A, Rissanen T, Hurme S, Kortela E, Hytönen J, Karonen M.

Ticks Tick Borne Dis

PMID:42001681

Free PMC article

Lyme neuroborreliosis (LNB), a disseminated manifestation of Lyme borreliosis (LB), arises when Borrelia burgdorferi sensu lato (Bbsl) spirochetes disseminate within the host and damage the peripheral nervous system and meninges, and in rare cases, also the parenchyma of the central nervous system (CNS). While early-stage LB is diagnosed clinically, accurate diagnosis of LNB requires cerebrospinal fluid (CSF) analysis, demonstrating pleocytosis and intrathecal synthesis of Bbsl-specific antibodies. There are, however, limitations in current LNB diagnostics, such as the unspecific nature of pleocytosis and post-treatment persistence of intrathecal antibodies necessitating the search for novel biomarkers. In this study, we employed untargeted ultrahigh-performance liquid chromatography coupled with tandem mass spectrometry (UHPLC-MS/MS) to profile small metabolites (<1500 Da) in CSF samples from subjects with definite acute LNB. Comparative analyses of metabolite profiles were performed between pretreatment subject samples (n = 63) and the following groups: (A) a subset of samples collected three weeks after treatment initiation from the same individuals (n = 36), (B) Bbsl antibody-negative subjects (non-LNB, n = 61), (C) subjects with other CNS infections (n = 21). Additionally, pretreatment LNB samples were compared between individuals with radiculitis (n = 40) and those without radiculitis (n = 23) (D). Out of 4222 molecular features (MFs) detected, 131 were prioritized based on statistical significance and magnitude of change for further detailed structural characterization. Altered metabolite classes included compounds from lysophospholipids [e.g., lysophosphatidylcholine (16:0), and lysophosphatidylethanolamine (18:0)], sphingomyelins [e.g., sphingomyelin (d18:1/14:0) and sphingomyelin d16:1/16:0)], sphingoid bases (e.g., d19:0 sphinganine, and 3-ketosphingosine), fatty acid amides (e.g., palmitoleamide and oleamide), cyclic phosphatidic acids [i.e., cyclic phosphatidic acid (16:0) and cyclic phosphatidic acid (18:2)], and amino acid metabolism (i.e., DL-glutamine, 5-hydroxytryptophan and DL-kynurenine). These findings underscore the potential of CSF metabolomics as a powerful complementary tool for diagnosing LNB and differentiating it from other CNS conditions. The identified metabolic signatures offer a foundation for future biomarker development and may enhance diagnostic precision, guide treatment strategies, and deepen our understanding of LNB pathogenesis.

Isotope Dilution NanoLC-MS/MS Quantitation of Methylglyoxal DNA-Protein Cross-Links: Formation and Repair in Human Cells.

Omondi RO, Barnes EM, Gurajala KC, Fisette G, Chaudray IA, Erber L.

Anal Chem

PMID:41995195

Free PMC article

DNA-protein cross-links (DPCs) represent a prevalent form of DNA damage that forms when cellular proteins become covalently trapped to DNA strands upon exposure to various endogenous and exogenous agents. Methylglyoxal is an endogenous metabolite that reacts with guanine and adenine bases in DNA and RNA, as well as cysteine, arginine, and lysine residues in proteins, generating advanced glycation end-products (AGEs), including DPCs. These modifications have been linked to human disease, including cancer, liver disease, diabetes, and neurodegenerative disorders. Herein, we present a mass spectrometry method for quantifying MGO-induced DNA-protein cross-links (DPCs) in human cells. We prepared an isotope 15 N 2 13 C 6 -dG-MGO-Lys internal standard and developed a quantitative liquid chromatography-tandem mass spectrometry (LC-MS/MS) method for detecting and quantifying the formation and repair of dG-MGO-Lys DPCs in cells. Genomic DNA was extracted, subjected to sequential protease and nuclease digestion, purified by offline high-performance liquid chromatography (HPLC), and analyzed by LC-MS/MS. The method's standard curve showed a strong linear relationship across a concentration range of 10-1000 fmol ( R 2 = 0.9994). The method achieved limits of detection (LOD) and quantification (LOQ) of 10 and 20 fmol, respectively. Inhibition of proteasome and SPRTN activity revealed that SPRTN functions as a predominant proteolytic enzyme in MGO DPC repair. Overall, this analytical approach can offer valuable insights into the relevance of DPCs in diseases linked to elevated MGO levels.

Label-Free High-Throughput Screening of CYP3A4 Inhibitors Using Acoustic Ejection Mass Spectrometry.

Rimmer MA, Wang J, Ranathunge TA, Shi Z, Li Y, Lee D, Chai SC, Lin W, Twarog NR, Ansari AZ, Shelat AA, Young BM, Chen T, Yang L.

Anal Chem

PMID:41997578

Free PMC article

Label-free high-throughput screening (HTS) technologies have greatly accelerated early drug discovery by allowing direct measurement of biochemical activity without the need for chemical labels. Techniques like MALDI-TOF, RapidFire, desorption electrospray ionization, and acoustic-mist ionization mass spectrometry have shown strong analytical performance. More recently, acoustic droplet ejection mass spectrometry (AEMS) has emerged as a next-generation platform capable of analyzing over a thousand data points per hour. In this study, we thoroughly evaluated an AEMS workflow using cytochrome P450 3A4 (CYP3A4) as a model enzyme. Screening a library of 9702 compounds, this work represents the first successful label-free HTS campaign for CYP3A4 inhibitors in a 384-well format using AEMS. The result using nifedipine as a substrate was comparable to the widely used P450-Glo luminescence assay but with fewer inhibitor hits identifications. To further compare and parse differences between the methods and the substrates, 819 hits were retested using AEMS with luciferin isopropyl acetal, the same substrate used in the luminescence assay. The findings confirmed that both the assay method and the substrate influence which inhibitors were detected. Overall, this study established AEMS as a robust and reliable tool for CYP3A4 inhibitor screening. It offers high analytical precision, fewer false positives, compatibility with multiple substrates, and direct detection of metabolites, providing a practical way to validate hits and improve confidence in early drug discovery efforts.

Quantification of the Active Metabolites 4-Methylaminoantipyrine and 4-Aminoantipyrine of Dipyrone From Human Plasma by LC-MS/MS.

Schmidt S, Ihmsen H, Golditz T, Schüttler J, Wehrfritz A.

Int J Anal Chem

PMID:42004449

Free PMC article

Dipyrone (metamizole) is widely used as a nonopioid analgesic in perioperative and intensive care settings; however, its administration may be associated with severe adverse effects. In this study, we describe an analytical assay for the quantification of the active metabolites 4-methylaminoantipyrine (4-MAA) and 4-aminoantipyrine (4-AA) in human plasma using ultra-high-performance liquid chromatography coupled with tandem mass spectrometry (UPLC-MS/MS). In addition, the protein-unbound fractions of both metabolites were determined by ultrafiltration. Chromatographic separation was performed on a UPLC system using gradient elution, followed by MS/MS detection with an electrospray ionization source. The limits of detection for both metabolites were 100 ng/mL. Across the investigated concentration range (100-10,000 ng/mL), the relative error (%RE) ranged from -6.3% to +3.5%. Intra-day and inter-assay variability were below 10%. Method validation was conducted in accordance with the 2018 FDA Bioanalytical Method Validation Guidance, and all evaluated parameters met the required criteria for analytical accuracy and precision. The developed assay is suitable for monitoring dipyrone metabolites and may support the prevention of potential overdosing during prolonged analgesic therapy or in intensive care settings.

Metabolomics profiling of acute myelogenous leukemia patients to identify systemic differences associated with in vitro sensitivity to SYK inhibitors.

Brattås MK, Hatfield KJ, Paulsen Rye K, Reikvam H.

Metabolomics

PMID:41995902

Free PMC article

Introduction Acute myelogenous leukemia (AML) is a heterogeneous hematological malignancy. Despite therapeutic advances, high relapse rates and poor survival persist, underscoring the need for new treatment strategies. Spleen tyrosine kinase (SYK) is crucial for leukemic cell survival and proliferation, and SYK inhibition is being explored in AML therapy. Objective This study aimed to identify whether distinct baseline serum metabolic profiles can differentiate between AML patient samples exhibiting high versus low in vitro sensitivity to SYK inhibition. Methods Leukemic cells from 49 AML patients were evaluated for their in vitro antiproliferative response to SYK-selective inhibitors (entospletinib, RO9021) and dual SYK/FLT3 inhibitors (fostamatinib, TAK-659). Serum samples from the same patients were subjected to untargeted metabolomic profiling using liquid chromatography-mass spectrometry (LC-MS). Bioinformatic analyses were applied to identify metabolic signatures associated with differential drug sensitivity. Results Hierarchical clustering identified three drug sensitivity groups, i.e. high, intermediate, low. Untargeted metabolomics identified 1204 metabolites across major pathways. Comparative analyses revealed distinct metabolic differences between patients with high versus low sensitivity to SYK inhibitors. For dual SYK/FLT3 inhibitors, lipid metabolites consistently were more discriminative for drug response, while for SYK selective inhibitors the profiles were more heterogeneous. Pathway analyses highlighted alterations in amino acid, lipid, and xenobiotic metabolism, including arginine biosynthesis and glycine/serine metabolism, as potential determinators for effect of SYK inhibition. Conclusion This study highlights potential metabolite signatures associated with in vitro SYK-targeted therapy in AML. These findings support future research to identify potential serum biomarkers, guiding personalized SYK inhibition strategies in AML.